RBR Ubiquitin Ligases: Diversification and Streamlining in Animal Lineages
نویسندگان
چکیده
منابع مشابه
Diversification and Specialization of Plant RBR Ubiquitin Ligases
BACKGROUND RBR ubiquitin ligases are components of the ubiquitin-proteasome system present in all eukaryotes. They are characterized by having the RBR (RING - IBR - RING) supradomain. In this study, the patterns of emergence of RBR genes in plants are described. METHODOLOGY/PRINCIPAL FINDINGS Phylogenetic and structural data confirm that just four RBR subfamilies (Ariadne, ARA54, Plant I/Heli...
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The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes. This unique family of E3 ligases includes parkin, whose dysfunction is linked to the pathogenesis of early-onset Parkinson's disease, and HOIP (HOIL-1-interacting protein) and HOIL-1 (haem-oxidized IRP2 ubiquitin ligase 1), m...
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Mutations in the parkin gene cause autosomal-recessive juvenile parkinsonism. Parkin encodes a ubiquitin-protein ligase characterized by having the RBR domain, composed of two RING fingers plus an IBR/DRIL domain. The RBR family is defined as the group of genes whose products contain an RBR domain. RBR family members exist in all eukaryotic species for which significant sequence data is availab...
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Most proteins of the TRIM family (also known as RBCC family) are ubiquitin ligases that share a peculiar protein structure, characterized by including an N-terminal RING finger domain closely followed by one or two B-boxes. Additional protein domains found at their C termini have been used to classify TRIM proteins into classes. TRIMs are involved in multiple cellular processes and many of them...
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The RING-in-between-RING (RBR) E3s are a curious family of ubiquitin E3-ligases, whose mechanism of action is unusual in several ways. Their activities are auto-inhibited, causing a requirement for activation by protein-protein interactions or posttranslational modifications. They catalyse ubiquitin conjugation by a concerted RING/HECT-like mechanism in which the RING1 domain facilitates E2-dis...
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ژورنال
عنوان ژورنال: Journal of Molecular Evolution
سال: 2009
ISSN: 0022-2844,1432-1432
DOI: 10.1007/s00239-009-9252-3